ROO_MEGG1
ID ROO_MEGG1 Reviewed; 402 AA.
AC Q9F0J6;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Rubredoxin-oxygen oxidoreductase;
DE Short=ROO;
DE Short=Rubredoxin oxidase;
DE EC=1.-.-.-;
GN Name=roo;
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=9278402; DOI=10.1074/jbc.272.36.22502;
RA Gomes C.M., Silva G., Oliveira S., LeGall J., Liu M.-Y., Xavier A.V.,
RA Rodrigues-Pousada C., Teixeira M.;
RT "Studies on the redox centers of the terminal oxidase from Desulfovibrio
RT gigas and evidence for its interaction with rubredoxin.";
RL J. Biol. Chem. 272:22502-22508(1997).
RN [2]
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=8503894; DOI=10.1006/bbrc.1993.1595;
RA Chen L., Liu M.-Y., LeGall J., Fareleira P., Santos H., Xavier A.V.;
RT "Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen
RT reduction to water by the 'strict anaerobe' Desulfovibrio gigas.";
RL Biochem. Biophys. Res. Commun. 193:100-105(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=11062560; DOI=10.1038/80961;
RA Frazao C., Silva G., Gomes C.M., Matias P., Coelho R., Sieker L.,
RA Macedo S., Liu M.-Y., Oliveira S., Teixeira M., Xavier A.V.,
RA Rodrigues-Pousada C., Carrondo M.A., Le Gall J.;
RT "Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.";
RL Nat. Struct. Biol. 7:1041-1045(2000).
CC -!- FUNCTION: Catalyzes the four-electron reduction of one oxygen molecule
CC to two water molecules.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:8503894};
CC Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:8503894};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:8503894};
CC Note=Binds 2 iron ions per monomer. {ECO:0000269|PubMed:8503894};
CC -!- PATHWAY: Energy metabolism; electron transfer.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8503894}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
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DR EMBL; AF218053; AAG34792.1; -; Genomic_DNA.
DR RefSeq; WP_021760300.1; NZ_AUBO01000056.1.
DR PDB; 1E5D; X-ray; 2.50 A; A/B=1-402.
DR PDBsum; 1E5D; -.
DR AlphaFoldDB; Q9F0J6; -.
DR SMR; Q9F0J6; -.
DR STRING; 1121448.DGI_1622; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR OMA; HVKNNIH; -.
DR UniPathway; UPA00092; -.
DR EvolutionaryTrace; Q9F0J6; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Flavoprotein; FMN; Iron; Metal-binding;
KW Oxidoreductase; Transport.
FT CHAIN 1..402
FT /note="Rubredoxin-oxygen oxidoreductase"
FT /id="PRO_0000216792"
FT DOMAIN 255..393
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 30..216
FT /note="Zinc metallo-hydrolase"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:1E5D"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1E5D"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1E5D"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1E5D"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:1E5D"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1E5D"
FT HELIX 379..400
FT /evidence="ECO:0007829|PDB:1E5D"
SQ SEQUENCE 402 AA; 44796 MW; 50E8A87481A6B2D9 CRC64;
MQATKIIDGF HLVGAIDWNS RDFHGYTLSP MGTTYNAYLV EDEKTTLFDT VKAEYKGELL
CGIASVIDPK KIDYLVIQHL ELDHAGALPA LIEACQPEKI FTSSLGQKAM ESHFHYKDWP
VQVVKHGETL SLGKRTVTFY ETRMLHWPDS MVSWFADEKV LISNDIFGQN IAASERFSDQ
IPVHTLERAM REYYANIVNP YAPQTLKAIE TLVGAGVAPE FICPDHGVIF RGADQCTFAV
QKYVEYAEQK PTNKVVIFYD SMWHSTEKMA RVLAESFRDE GCTVKLMWCK ACHHSQIMSE
ISDAGAVIVG SPTHNNGILP YVAGTLQYIK GLRPQNKIGG AFGSFGWSGE STKVLAEWLT
GMGFDMPATP VKVKNVPTHA DYEQLKTMAQ TIARALKAKL AA
